ID E6N6A6_CALS0 Unreviewed; 576 AA.
AC E6N6A6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Acetolactate synthase {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
GN ORFNames=CSUB_C0816 {ECO:0000313|EMBL:BAJ50673.1}, HGMM_F52H05C34
GN {ECO:0000313|EMBL:BAJ47825.1};
OS Caldiarchaeum subterraneum.
OC Archaea; Nitrososphaerota; Candidatus Caldarchaeales;
OC Candidatus Caldarchaeaceae; Candidatus Caldarchaeum.
OX NCBI_TaxID=311458 {ECO:0000313|EMBL:BAJ47825.1, ECO:0000313|Proteomes:UP000008120};
RN [1] {ECO:0000313|EMBL:BAJ47825.1, ECO:0000313|Proteomes:UP000008120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAJ47825.1, ECO:0000313|Proteomes:UP000008120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21169198; DOI=10.1093/nar/gkq1228;
RA Nunoura T., Takaki Y., Kakuta J., Nishi S., Sugahara J., Kazama H.,
RA Chee G., Hattori M., Kanai A., Atomi H., Takai K., Takami H.;
RT "Insights into the evolution of Archaea and eukaryotic protein modifier
RT systems revealed by the genome of a novel archaeal group.";
RL Nucleic Acids Res. 39:3204-3223(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU003591};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU003591};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974, ECO:0000256|RuleBase:RU003591}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC ECO:0000256|RuleBase:RU003591}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU003591}.
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DR EMBL; AP011847; BAJ47825.1; -; Genomic_DNA.
DR EMBL; BA000048; BAJ50673.1; -; Genomic_DNA.
DR AlphaFoldDB; E6N6A6; -.
DR STRING; 311458.CSUB_C0816; -.
DR KEGG; csu:CSUB_C0816; -.
DR BioCyc; CCAL311458:G131R-828-MONOMER; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000008120; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02015; TPP_AHAS; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR012846; Acetolactate_synth_lsu.
DR InterPro; IPR039368; AHAS_TPP.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR00118; acolac_lg; 1.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU003591};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU003591}; Magnesium {ECO:0000256|RuleBase:RU003591};
KW Metal-binding {ECO:0000256|RuleBase:RU003591};
KW Reference proteome {ECO:0000313|Proteomes:UP000008120};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:BAJ47825.1}.
FT DOMAIN 1..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..535
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 576 AA; 63102 MW; 091150FD73385C7F CRC64;
MRAADALVKM MEKKGVEYVF GIPGGANMPF YDALRDSDIK SILMRHEQQA AHAAEGYGRV
KRRPGICSGT SGPGATNLIT GLVDAYMDSS PVVAITGQVV RSFMGTDAFQ EADIVGLVLP
HIKYAVTVKD PHRVLQEFVN AYHIAAHHRP GPTLLDLPRD VFMEEVEENY DIQPEPLFNR
PLPEPDIESI KQAAKLIAEA EKPVLLVGGG AVYSMAGKEI LELAEHIAAP IVTTTMGKGA
VPEDHPLVLG VVGMHGRVEA DLAIVESDLV ICIGSRLSDR AIGPAKEFEK NRKTIHIDID
ASEFGKNVRP TVSLPGDARK VLAELVEYTK AIVARRPECQ LAKKLREIGE AYEEYMMAMD
DGRVLHSWKV VSLLTDAVPP DTIVSTGVGQ HQMWAQLFWK NRTPGTWLTS GGLGTMGFGL
PAAFGAKAAA PDRIVMNLDG DGSFLMTCQT LACVADYDLP VITVIFDNRS LGMVKQWQDM
FYNKRYKDVE YNDRTDLVKL SEAFGVEAVR VESYDELLKV VMRAVRTNSA LTVDVPVDTG
ELVFPMVPPG RWLEDVKLPP GFDLSQRMVA AGRMST
//
